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Q86W56

- PARG_HUMAN

UniProt

Q86W56 - PARG_HUMAN

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Protein

Poly(ADP-ribose) glycohydrolase

Gene

PARG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters.1 Publication

Catalytic activityi

Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei737 – 73711 Publication
Binding sitei740 – 7401Substrate
Binding sitei754 – 7541Substrate; via amide nitrogen
Active sitei755 – 75511 Publication
Active sitei756 – 75611 Publication
Binding sitei795 – 7951SubstrateBy similarity

GO - Molecular functioni

  1. poly(ADP-ribose) glycohydrolase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(ADP-ribose) glycohydrolase (EC:3.2.1.143)
Gene namesi
Name:PARG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:8605. PARG.

Subcellular locationi

Isoform 1 : Nucleus 2 Publications
Note: Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage.
Isoform 2 : Cytoplasm 1 Publication
Note: Translocates to the nucleus in response to DNA damage.

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. mitochondrion Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121K → A: Abolishes nuclear targeting; when associated with G-13. 1 Publication
Mutagenesisi13 – 131R → G: Abolishes nuclear targeting; when associated with A-12. 1 Publication
Mutagenesisi36 – 361R → A: No effect. 1 Publication
Mutagenesisi37 – 371R → G: No effect. 1 Publication

Organism-specific databases

PharmGKBiPA32940.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 976976Poly(ADP-ribose) glycohydrolasePRO_0000066602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei133 – 1331Phosphoserine1 Publication
Modified residuei137 – 1371Phosphoserine1 Publication
Modified residuei197 – 1971Phosphoserine3 Publications
Modified residuei199 – 1991Phosphothreonine3 Publications
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei264 – 2641PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei298 – 2981Phosphoserine1 Publication
Modified residuei302 – 3021Phosphoserine1 Publication
Modified residuei340 – 3401N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ86W56.
PaxDbiQ86W56.
PRIDEiQ86W56.

PTM databases

PhosphoSiteiQ86W56.

Miscellaneous databases

PMAP-CutDBQ86W56.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ86W56.
CleanExiHS_PARG.
ExpressionAtlasiQ86W56. baseline and differential.
GenevestigatoriQ86W56.

Organism-specific databases

HPAiHPA021819.

Interactioni

Subunit structurei

Interacts with PCNA.2 Publications

Protein-protein interaction databases

BioGridi114077. 3 interactions.
IntActiQ86W56. 1 interaction.
STRINGi9606.ENSP00000384408.

Structurei

Secondary structure

1
976
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi452 – 4565Combined sources
Helixi458 – 4603Combined sources
Turni464 – 4674Combined sources
Beta strandi480 – 4823Combined sources
Helixi486 – 4883Combined sources
Beta strandi497 – 5015Combined sources
Beta strandi520 – 5223Combined sources
Beta strandi532 – 5343Combined sources
Helixi535 – 5439Combined sources
Helixi550 – 55910Combined sources
Helixi562 – 5643Combined sources
Turni565 – 5673Combined sources
Helixi571 – 5799Combined sources
Helixi583 – 5919Combined sources
Helixi593 – 60210Combined sources
Helixi604 – 6074Combined sources
Beta strandi621 – 6266Combined sources
Helixi627 – 63812Combined sources
Turni652 – 6554Combined sources
Helixi662 – 6654Combined sources
Helixi672 – 68817Combined sources
Beta strandi694 – 7018Combined sources
Helixi708 – 7103Combined sources
Beta strandi718 – 7247Combined sources
Helixi726 – 7294Combined sources
Turni730 – 7323Combined sources
Beta strandi733 – 7397Combined sources
Turni743 – 7508Combined sources
Helixi754 – 7618Combined sources
Helixi763 – 7675Combined sources
Helixi768 – 7714Combined sources
Beta strandi779 – 7846Combined sources
Beta strandi790 – 7934Combined sources
Helixi796 – 7983Combined sources
Beta strandi800 – 8045Combined sources
Beta strandi815 – 8184Combined sources
Beta strandi820 – 8256Combined sources
Helixi832 – 8365Combined sources
Helixi838 – 85215Combined sources
Helixi859 – 8613Combined sources
Beta strandi865 – 8684Combined sources
Helixi873 – 8753Combined sources
Helixi879 – 89214Combined sources
Beta strandi897 – 9004Combined sources
Helixi905 – 92016Combined sources
Helixi925 – 93915Combined sources
Turni940 – 9423Combined sources
Beta strandi945 – 9473Combined sources
Helixi952 – 96110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A0DX-ray1.75A448-976[»]
4B1GX-ray1.83A448-976[»]
4B1HX-ray2.00A448-976[»]
4B1IX-ray2.14A448-976[»]
4B1JX-ray2.08A448-976[»]
ProteinModelPortaliQ86W56.
SMRiQ86W56. Positions 450-963.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 456456A-domainAdd
BLAST
Regioni610 – 795186CatalyticAdd
BLAST
Regioni726 – 7272Substrate binding
Regioni869 – 8746Substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi10 – 167Nuclear localization signal1 Publication
Motifi76 – 838PIP-box (PCNA interacting peptide)

Domaini

The PIP-box mediates interaction with PCNA and localization to replication foci.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG254589.
GeneTreeiENSGT00390000003652.
HOVERGENiHBG053510.
InParanoidiQ86W56.
KOiK07759.
PhylomeDBiQ86W56.
TreeFamiTF323527.

Family and domain databases

InterProiIPR007724. Poly_GlycHdrlase.
[Graphical view]
PANTHERiPTHR12837. PTHR12837. 1 hit.
PfamiPF05028. PARG_cat. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86W56-1) [UniParc]FASTAAdd to Basket

Also known as: hPARG111

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNAGPGCEPC TKRPRWGAAT TSPAASDARS FPSRQRRVLD PKDAHVQFRV
60 70 80 90 100
PPSSPACVPG RAGQHRGSAT SLVFKQKTIT SWMDTKGIKT AESESLDSKE
110 120 130 140 150
NNNTRIESMM SSVQKDNFYQ HNVEKLENVS QLSLDKSPTE KSTQYLNQHQ
160 170 180 190 200
TAAMCKWQNE GKHTEQLLES EPQTVTLVPE QFSNANIDRS PQNDDHSDTD
210 220 230 240 250
SEENRDNQQF LTTVKLANAK QTTEDEQARE AKSHQKCSKS CDPGEDCASC
260 270 280 290 300
QQDEIDVVPE SPLSDVGSED VGTGPKNDNK LTRQESCLGN SPPFEKESEP
310 320 330 340 350
ESPMDVDNSK NSCQDSEADE ETSPGFDEQE DGSSSQTANK PSRFQARDAD
360 370 380 390 400
IEFRKRYSTK GGEVRLHFQF EGGESRTGMN DLNAKLPGNI SSLNVECRNS
410 420 430 440 450
KQHGKKDSKI TDHFMRLPKA EDRRKEQWET KHQRTERKIP KYVPPHLSPD
460 470 480 490 500
KKWLGTPIEE MRRMPRCGIR LPLLRPSANH TVTIRVDLLR AGEVPKPFPT
510 520 530 540 550
HYKDLWDNKH VKMPCSEQNL YPVEDENGER TAGSRWELIQ TALLNKFTRP
560 570 580 590 600
QNLKDAILKY NVAYSKKWDF TALIDFWDKV LEEAEAQHLY QSILPDMVKI
610 620 630 640 650
ALCLPNICTQ PIPLLKQKMN HSITMSQEQI ASLLANAFFC TFPRRNAKMK
660 670 680 690 700
SEYSSYPDIN FNRLFEGRSS RKPEKLKTLF CYFRRVTEKK PTGLVTFTRQ
710 720 730 740 750
SLEDFPEWER CEKPLTRLHV TYEGTIEENG QGMLQVDFAN RFVGGGVTSA
760 770 780 790 800
GLVQEEIRFL INPELIISRL FTEVLDHNEC LIITGTEQYS EYTGYAETYR
810 820 830 840 850
WSRSHEDGSE RDDWQRRCTE IVAIDALHFR RYLDQFVPEK MRRELNKAYC
860 870 880 890 900
GFLRPGVSSE NLSAVATGNW GCGAFGGDAR LKALIQILAA AAAERDVVYF
910 920 930 940 950
TFGDSELMRD IYSMHIFLTE RKLTVGDVYK LLLRYYNEEC RNCSTPGPDI
960 970
KLYPFIYHAV ESCAETADHS GQRTGT
Length:976
Mass (Da):111,110
Last modified:June 1, 2003 - v1
Checksum:iD6646353C6D0180E
GO
Isoform 2 (identifier: Q86W56-2) [UniParc]FASTAAdd to Basket

Also known as: hPARG102

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.

Show »
Length:894
Mass (Da):102,312
Checksum:i666B77E891E4A500
GO
Isoform 3 (identifier: Q86W56-3) [UniParc]FASTAAdd to Basket

Also known as: hPARG99

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Show »
Length:868
Mass (Da):99,432
Checksum:i85BCE7201ABABA5F
GO
Isoform 4 (identifier: Q86W56-4) [UniParc]FASTAAdd to Basket

Also known as: hPARG60

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MNAGPGCEPCTKRPR → MVQAGAEKDAQSISL
     16-423: Missing.
     485-526: RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE → W

Note: Catalytically inactive.

Show »
Length:527
Mass (Da):60,873
Checksum:i0FBB26152C56D33D
GO
Isoform 5 (identifier: Q86W56-5) [UniParc]FASTAAdd to Basket

Also known as: hPARG55

The sequence of this isoform differs from the canonical sequence as follows:
     1-460: Missing.
     485-526: RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE → W

Note: Catalytically inactive.

Show »
Length:475
Mass (Da):54,794
Checksum:i5443EFFA21AA84CE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 142RP → AT in AAB61614. (PubMed:10449915)Curated
Sequence conflicti61 – 611R → Q in AAB61614. (PubMed:10449915)Curated
Sequence conflicti127 – 1271E → V in AAB61614. (PubMed:10449915)Curated
Sequence conflicti138 – 1381P → L in AAB61614. (PubMed:10449915)Curated
Sequence conflicti227 – 2271Q → H in AAB61614. (PubMed:10449915)Curated
Sequence conflicti242 – 2421D → H in AAB61614. (PubMed:10449915)Curated
Sequence conflicti260 – 2601E → K in AAB61614. (PubMed:10449915)Curated
Sequence conflicti275 – 2751P → S in AAB61614. (PubMed:10449915)Curated
Sequence conflicti282 – 2821T → I in AAB61614. (PubMed:10449915)Curated
Sequence conflicti414 – 4141F → L in AAB61614. (PubMed:10449915)Curated
Sequence conflicti466 – 4661R → Q in AFM56043. (PubMed:22433848)Curated
Sequence conflicti484 – 4841I → V in AFM56043. (PubMed:22433848)Curated
Sequence conflicti814 – 8152WQ → CE in AAB61614. (PubMed:10449915)Curated
Sequence conflicti817 – 8171R → H in AAH52966. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 460460Missing in isoform 5. 1 PublicationVSP_044674Add
BLAST
Alternative sequencei1 – 108108Missing in isoform 3. 2 PublicationsVSP_011770Add
BLAST
Alternative sequencei1 – 8282Missing in isoform 2. 2 PublicationsVSP_011769Add
BLAST
Alternative sequencei1 – 1515MNAGP…TKRPR → MVQAGAEKDAQSISL in isoform 4. 1 PublicationVSP_044675Add
BLAST
Alternative sequencei16 – 423408Missing in isoform 4. 1 PublicationVSP_044676Add
BLAST
Alternative sequencei485 – 52642RVDLL…PVEDE → W in isoform 4 and isoform 5. 2 PublicationsVSP_044677Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY258587 mRNA. Translation: AAP83314.1.
AY575848 mRNA. Translation: AAT66421.1.
AY575849 mRNA. Translation: AAT66422.1.
AF005043 mRNA. Translation: AAB61614.1.
EF382674 mRNA. Translation: ABR10027.1.
JQ890226 mRNA. Translation: AFM56043.1.
AK295786 mRNA. Translation: BAG58607.1.
AK302560 mRNA. Translation: BAG63826.1.
AK314909 mRNA. Translation: BAG37421.1.
BC050560 mRNA. Translation: AAH50560.1.
BC052966 mRNA. Translation: AAH52966.1.
CCDSiCCDS73130.1. [Q86W56-1]
RefSeqiNP_003622.2. NM_003631.2. [Q86W56-1]
UniGeneiHs.10136.
Hs.535298.
Hs.732225.

Genome annotation databases

EnsembliENST00000402038; ENSP00000384408; ENSG00000227345. [Q86W56-1]
ENST00000616448; ENSP00000484285; ENSG00000227345. [Q86W56-1]
GeneIDi8505.
KEGGihsa:8505.
UCSCiuc001jif.3. human. [Q86W56-1]
uc010qgx.2. human. [Q86W56-3]

Polymorphism databases

DMDMi56417893.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY258587 mRNA. Translation: AAP83314.1 .
AY575848 mRNA. Translation: AAT66421.1 .
AY575849 mRNA. Translation: AAT66422.1 .
AF005043 mRNA. Translation: AAB61614.1 .
EF382674 mRNA. Translation: ABR10027.1 .
JQ890226 mRNA. Translation: AFM56043.1 .
AK295786 mRNA. Translation: BAG58607.1 .
AK302560 mRNA. Translation: BAG63826.1 .
AK314909 mRNA. Translation: BAG37421.1 .
BC050560 mRNA. Translation: AAH50560.1 .
BC052966 mRNA. Translation: AAH52966.1 .
CCDSi CCDS73130.1. [Q86W56-1 ]
RefSeqi NP_003622.2. NM_003631.2. [Q86W56-1 ]
UniGenei Hs.10136.
Hs.535298.
Hs.732225.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4A0D X-ray 1.75 A 448-976 [» ]
4B1G X-ray 1.83 A 448-976 [» ]
4B1H X-ray 2.00 A 448-976 [» ]
4B1I X-ray 2.14 A 448-976 [» ]
4B1J X-ray 2.08 A 448-976 [» ]
ProteinModelPortali Q86W56.
SMRi Q86W56. Positions 450-963.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114077. 3 interactions.
IntActi Q86W56. 1 interaction.
STRINGi 9606.ENSP00000384408.

Chemistry

BindingDBi Q86W56.
ChEMBLi CHEMBL1795143.

PTM databases

PhosphoSitei Q86W56.

Polymorphism databases

DMDMi 56417893.

Proteomic databases

MaxQBi Q86W56.
PaxDbi Q86W56.
PRIDEi Q86W56.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000402038 ; ENSP00000384408 ; ENSG00000227345 . [Q86W56-1 ]
ENST00000616448 ; ENSP00000484285 ; ENSG00000227345 . [Q86W56-1 ]
GeneIDi 8505.
KEGGi hsa:8505.
UCSCi uc001jif.3. human. [Q86W56-1 ]
uc010qgx.2. human. [Q86W56-3 ]

Organism-specific databases

CTDi 8505.
GeneCardsi GC10M051026.
H-InvDB HIX0127080.
HGNCi HGNC:8605. PARG.
HPAi HPA021819.
MIMi 603501. gene.
neXtProti NX_Q86W56.
PharmGKBi PA32940.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG254589.
GeneTreei ENSGT00390000003652.
HOVERGENi HBG053510.
InParanoidi Q86W56.
KOi K07759.
PhylomeDBi Q86W56.
TreeFami TF323527.

Miscellaneous databases

ChiTaRSi PARG. human.
GeneWikii PARG.
GenomeRNAii 8505.
NextBioi 31829.
PMAP-CutDB Q86W56.
PROi Q86W56.
SOURCEi Search...

Gene expression databases

Bgeei Q86W56.
CleanExi HS_PARG.
ExpressionAtlasi Q86W56. baseline and differential.
Genevestigatori Q86W56.

Family and domain databases

InterProi IPR007724. Poly_GlycHdrlase.
[Graphical view ]
PANTHERi PTHR12837. PTHR12837. 1 hit.
Pfami PF05028. PARG_cat. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23)."
    Meyer R.G., Meyer-Ficca M.L., Jacobson E.L., Jacobson M.K.
    Gene 314:181-190(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Skin.
  2. "Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments."
    Meyer-Ficca M.L., Meyer R.G., Coyle D.L., Jacobson E.L., Jacobson M.K.
    Exp. Cell Res. 297:521-532(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), MUTAGENESIS OF LYS-12; ARG-13; ARG-36 AND ARG-37, NUCLEAR LOCALIZATION SIGNAL.
    Tissue: Skin.
  3. "Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization."
    Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K.
    Cytogenet. Cell Genet. 85:269-270(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity."
    Meyer R.G., Meyer-Ficca M.L., Whatcott C.J., Jacobson E.L., Jacobson M.K.
    Exp. Cell Res. 313:2920-2936(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION.
    Tissue: Testis.
  5. "ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose)."
    Niere M., Mashimo M., Agledal L., Dolle C., Kasamatsu A., Kato J., Moss J., Ziegler M.
    J. Biol. Chem. 287:16088-16102(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORMS 4 AND 5), ABSENCE OF CATALYTIC ACTIVITY (ISOFORMS 4 AND 5), SUBCELLULAR LOCATION.
    Tissue: Peripheral blood monocyte.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Brain cortex, Hippocampus and Testis.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin and Testis.
  8. "Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage."
    Haince J.F., Ouellet M.E., McDonald D., Hendzel M.J., Poirier G.G.
    Biochim. Biophys. Acta 1763:226-237(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-137; SER-197 AND THR-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Proteomic investigation of phosphorylation sites in poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase."
    Gagne J.P., Moreel X., Gagne P., Labelle Y., Droit A., Chevalier-Pare M., Bourassa S., McDonald D., Hendzel M.J., Prigent C., Poirier G.G.
    J. Proteome Res. 8:1014-1029(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-197; THR-199 AND SER-298.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms."
    Mortusewicz O., Fouquerel E., Ame J.C., Leonhardt H., Schreiber V.
    Nucleic Acids Res. 39:5045-5056(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORM 1), INTERACTION WITH PCNA.
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated gene expression."
    Le May N., Iltis I., Ame J.C., Zhovmer A., Biard D., Egly J.M., Schreiber V., Coin F.
    Mol. Cell 48:785-798(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives."
    Tucker J.A., Bennett N., Brassington C., Durant S.T., Hassall G., Holdgate G., McAlister M., Nissink J.W., Truman C., Watson M.
    PLoS ONE 7:E50889-E50889(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 448-976 ALONE AND IN COMPLEX WITH INHIBITORS, ACTIVE SITE, SUBSTRATE-BINDING SITES.

Entry informationi

Entry nameiPARG_HUMAN
AccessioniPrimary (citable) accession number: Q86W56
Secondary accession number(s): A5YBK3
, B2RC24, B4DIU5, B4DYR4, I6RUV3, Q6E4P6, Q6E4P7, Q7Z742, Q9Y4W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3